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New sequence data enable modelling of the fungal alternative oxidase and explain an absence of regulation by pyruvate
Author(s) -
Joseph-Horne Tim,
Babij Joanna,
Wood Paul M,
Hollomon Derek,
Sessions Richard B
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01943-8
Subject(s) - alternative oxidase , biochemistry , biology , cysteine , ubiquinol , sequence (biology) , stereochemistry , chemistry , mitochondrion , enzyme , coenzyme q – cytochrome c reductase , cytochrome c
Respiratory rates involving the alternative oxidase (AO) were studied in mitochondria from Tapesia acuformis . There was no evidence for regulation by pyruvate, in contrast with plant AO. The site of interaction of pyruvate with the plant AO is a conserved cysteine. The primary sequence was obtained for AO from Magnaporthe grisea and compared with four published sequences for fungal AO. In all cases this cysteine was absent. Sequence data were obtained for the C‐terminal domain of a further five fungal AOs. In this region the fungal sequences were all consistent with a four‐helix, di‐iron binding structure as in the ferritin‐fold family. A molecular model of this domain was deduced from the structure of Δ‐9 desaturase. This is in general agreement with that developed for plant AOs, despite very low sequence identity between the two kingdoms. Further modelling indicated an appropriate active site for binding of ubiquinol, required in the AO redox reaction.